|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_FGGY_RhaB-like |
cd07771 |
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase ... |
8-466 |
0e+00 |
|
nucleotide-binding domain (NBD) of rhamnulokinase (RhaB) and similar proteins; Rhamnulokinase (EC 2.7.1.5), also known as L-rhamnulose kinase, ATP:L-rhamnulose phosphotransferase, L-rhamnulose 1-kinase, or rhamnulose kinase, is an enzyme involved in the second step in rhamnose catabolism. It catalyzes the ATP-dependent phosphorylation of L-rhamnulose to produce L-rhamnulose-1-phosphate and ADP. Rhamnulokinase exists as a monomer composed of two large domains. The ATP binding site is located in the cleft between the two domains. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The presence of divalent Mg2+ or Mn2+ is required for catalysis. The subfamily also includes Streptococcus pneumoniae L-fuculose k fuculose Kinase inase (FcsK) that uses ATP to phosphorylate fuculose creating fuculose-1-phosphate, and Alkalihalobacillus clausii bifunctional enzyme RhaA/RhaB. Members of this subfamily belong to the FGGY family of carbohydrate kinases.
Pssm-ID: 466791 [Multi-domain] Cd Length: 460 Bit Score: 663.46 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 8 TYLAADFGGGSGRIIAGFLHHGKLELEEVYRFCNRQVKLGNHIYWDFPALFEDMKTGLKLAAQKGYAVKSIGIDTWGVDF 87
Cdd:cd07771 1 NYLAVDLGASSGRVILGSLDGGKLELEEIHRFPNRPVEINGHLYWDIDRLFDEIKEGLKKAAEQGGDIDSIGIDTWGVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 88 GLIDKHGNLLGNPVCYRDARTEGIPEEVFKLLDERQHYADTGIQVMAINTLFQLYSMKQHQDAQLEVARQLLFMPDLFSY 167
Cdd:cd07771 81 GLLDKNGELLGNPVHYRDPRTEGMMEELFEKISKEELYERTGIQFQPINTLYQLYALKKEGPELLERADKLLMLPDLLNY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 168 FLTGVANNEYCIASTSELLDAQSRNWSVDTIRALGLPEHLFGEIILPGTIRGTLKEDIARETGLGTVDVIAVGSHDTASA 247
Cdd:cd07771 161 LLTGEKVAEYTIASTTQLLDPRTKDWSEELLEKLGLPRDLFPPIVPPGTVLGTLKPEVAEELGLKGIPVIAVASHDTASA 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 248 VAAVPAVENPIAFLSSGTWSLLGVEVDEPILTEEARKAQFTNEGGVDGKIRFLQNITGLWILQRLMSEWKACGEEQNYDI 327
Cdd:cd07771 241 VAAVPAEDEDAAFISSGTWSLIGVELDEPVITEEAFEAGFTNEGGADGTIRLLKNITGLWLLQECRREWEEEGKDYSYDE 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 328 IIPQAAEAQ-IATIIPVDDATFMNPENMENALIHYCRHHALQVPKNKAETVRCVLQSLAFKYRQAVEQLNHCLPSPIRQL 406
Cdd:cd07771 321 LVALAEEAPpFGAFIDPDDPRFLNPGDMPEAIRAYCRETGQPVPESPGEIARCIYESLALKYAKTIEELEELTGKRIDRI 400
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 407 NIIGGGSQNQLLNQLTADELGIPVYAGPVEATAMGNILTQAMAKGEIADLRELREIVTRS 466
Cdd:cd07771 401 HIVGGGSRNALLCQLTADATGLPVIAGPVEATAIGNLLVQLIALGEIKSLEEGRELVRNS 460
|
|
| rhamnulo_kin |
TIGR02627 |
rhamnulokinase; This model describes rhamnulokinase, an enzyme that catalyzes the second step ... |
10-466 |
3.19e-161 |
|
rhamnulokinase; This model describes rhamnulokinase, an enzyme that catalyzes the second step in rhamnose catabolism.
Pssm-ID: 274237 [Multi-domain] Cd Length: 454 Bit Score: 463.84 E-value: 3.19e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 10 LAADFGGGSGRIIAGFLHHG--KLELEEVYRFCNRQVKLGNHIYWDFPALFEDMKTGLKLAAQKGYAVKSIGIDTWGVDF 87
Cdd:TIGR02627 1 VAVDLGASSGRVMLASYENEcqKLTLEEIHRFKNGLVSQNGHECWDIDALEQEIRLGLNKVDAEGIAPDSIGIDTWGVDF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 88 GLIDKHGNLLGNPVCYRDARTEGIPEEVFKLLDERQHYADTGIQVMAINTLFQLYSMKQHQDAQLEVARQLLFMPDLFSY 167
Cdd:TIGR02627 81 VLLDQNGQRVGDPVSYRDSRTDGVMAQVQSELGKEAIYQRTGIQFLPFNTLYQLRALTEQQPDLLEKVAHFLLIPDYLNY 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 168 FLTGVANNEYCIASTSELLDAQSRNWSVDTIRALGLPEHLFGEIILPGTIRGTLKEDIAREtglgtVDVIAVGSHDTASA 247
Cdd:TIGR02627 161 RLTGKKVWEYTNATTTQLVNINTDDWDEDLLAYLGVPAAWFGRPTHPGNVIGLWECPQGNQ-----IPVVAVATHDTASA 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 248 VAAVPAVENPIAFLSSGTWSLLGVEVDEPILTEEARKAQFTNEGGVDGKIRFLQNITGLWILQRLmsewkaCGEEQNYDI 327
Cdd:TIGR02627 236 VVAAPLQGENAAYLSSGTWSLMGFESQTPITNEQALAANITNEGGADGRYRVLKNIMGLWLLQRV------CRERDINDL 309
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 328 -IIPQAAEAQIA--TIIPVDDATFMNPENMENALIHYCRHHALQVPKNKAETVRCVLQSLAFKYRQAVEQLNHCLPSPIR 404
Cdd:TIGR02627 310 pALIEQAQALPAfkSIINPNDDRFINPENMCEEIQAYCRETNQPIPESDAELARCIFDSLALLYRQVLLELAELRGKPIS 389
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1697055883 405 QLNIIGGGSQNQLLNQLTADELGIPVYAGPVEATAMGNILTQAMAKGEIADLRELREIVTRS 466
Cdd:TIGR02627 390 QLHIVGGGSQNAFLNQLCADACGIRVIAGPVEASTLGNIGVQLMALDEINDMAAFRQIVSNN 451
|
|
| rhaB |
PRK10640 |
rhamnulokinase; Provisional |
27-475 |
1.48e-138 |
|
rhamnulokinase; Provisional
Pssm-ID: 182609 [Multi-domain] Cd Length: 471 Bit Score: 406.80 E-value: 1.48e-138
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 27 HHGKLELEEVYRFCNRQVKLGNHIYWDFPALFEDMKTGLKLAAQKGYAVKSIGIDTWGVDFGLIDKHGNLLGNPVCYRDA 106
Cdd:PRK10640 8 ECRSLTLREIHRFNNGLHSQDGFDTWDVDSLESAIRLGLNKVCEEGIRIDSIGIDTWGVDYVLLDKQGQRVGLPVSYRDS 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 107 RTEGIPEEVFKLLDERQHYADTGIQVMAINTLFQLYSMKQHQDAQLEVARQLLFMPDLFSYFLTGVANNEYCIASTSELL 186
Cdd:PRK10640 88 RTDGVMAQAQQQLGKRDIYRRSGIQFLPFNTLYQLRALTEQQPELIAQVAHALLIPDYFSYRLTGKMNWEYTNATTTQLV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 187 DAQSRNWSVDTIRALGLPEHLFGEIILPGTIRGTLKEDIAREtglgtVDVIAVGSHDTASAVAAVPAVENPIAFLSSGTW 266
Cdd:PRK10640 168 NINSDDWDESLLAWSGAPKAWFGRPTHPGNVIGHWICPQGNE-----IPVVAVASHDTASAVIASPLNDSDAAYLSSGTW 242
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 267 SLLGVEVDEPILTEEARKAQFTNEGGVDGKIRFLQNITGLWILQRLmsewkaCGEEQNYDI--IIPQA-AEAQIATIIPV 343
Cdd:PRK10640 243 SLMGFESQTPFTNDTALAANITNEGGAEGRYRVLKNIMGLWLLQRV------LQERQITDLpaLIAATaALPACRFLINP 316
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 344 DDATFMNPENMENALIHYCRHHALQVPKNKAETVRCVLQSLAFKYRQAVEQLNHCLPSPIRQLNIIGGGSQNQLLNQLTA 423
Cdd:PRK10640 317 NDDRFINPPSMCSEIQAACRETAQPVPESDAELARCIFDSLALLYADVLHELAQLRGEPFSQLHIVGGGCQNALLNQLCA 396
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1697055883 424 DELGIPVYAGPVEATAMGNILTQAMAKGEIADLRELREIVTRSVTPQVYYPK 475
Cdd:PRK10640 397 DACGIRVIAGPVEASTLGNIGIQLMTLDELNNVDDFRQVVSTNFPLTTFTPN 448
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
51-441 |
3.95e-53 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 184.71 E-value: 3.95e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 51 YWDFPALFEDMKTGLK--LAAQKGYAVKSIGIDTWGVDFGLIDKHGNLLGNPVCYRDARTEGIPEEVFKLLDERQHYADT 128
Cdd:cd07773 42 ELDPEELWEAVKEAIReaAAQAGPDPIAAISVSSQGESGVPVDRDGEPLGPAIVWFDPRGKEEAEELAERIGAEELYRIT 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 129 GIQVMAINTLFQLYSMKQHQDAQLEVARQLLFMPDLFSYFLTGVANNEYCIASTSELLDAQSRNWSVDTIRALGLPEHLF 208
Cdd:cd07773 122 GLPPSPMYSLAKLLWLREHEPEIFAKAAKWLSVADYIAYRLTGEPVTDYSLASRTMLFDIRKRTWSEELLEAAGIDASLL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 209 GEIILPGTIRGTLKEDIARETGL--GTvdVIAVGSHDTASAVAAVPAVENPIAFLSSGTWSLLGVEVDEPILTEEARKAQ 286
Cdd:cd07773 202 PELVPSGTVIGTVTPEAAEELGLpaGT--PVVVGGHDHLCAALGAGVIEPGDVLDSTGTAEALLAVVDEPPLDEMLAEGG 279
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 287 FTNEGGVD-GKIRFLQNITGLWILQRLMSEWkaCGEEQNYDIIIPQAAEaqiatIIPVDDATFMNPeNMENALIHYCRHH 365
Cdd:cd07773 280 LSYGHHVPgGYYYLAGSLPGGALLEWFRDLF--GGDESDLAAADELAEA-----APPGPTGLLFLP-HLSGSGTPDFDPD 351
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 366 A------LQVPKNKAETVRCVLQSLAFKYRQAVEQLNHCLPsPIRQLNIIGGGSQNQLLNQLTADELGIPVYAGPV-EAT 438
Cdd:cd07773 352 ArgaflgLTLGTTRADLLRAILEGLAFELRLNLEALEKAGI-PIDEIRAVGGGARSPLWLQLKADILGRPIEVPEVpEAT 430
|
...
gi 1697055883 439 AMG 441
Cdd:cd07773 431 ALG 433
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
49-474 |
5.26e-45 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 163.66 E-value: 5.26e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 49 HIyWDFPALFEDM-----KTGLKLAAQKgyaVKSIGIDTWGVDFGLIDKHGNLLGNPVCYRDARTEGIPEEVFKLLDERQ 123
Cdd:PRK10331 45 HQ-WSLDAILQRFadccrQINSELTECH---IRGITVTTFGVDGALVDKQGNLLYPIISWKCPRTAAVMENIERYISAQQ 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 124 HYADTGIQVMAINTLFQLYSMKQHQDAQLEVARQLLFMPDLFSYFLTGVANNEYCIASTSELLDAQSRNWSVDTIRALGL 203
Cdd:PRK10331 121 LQQISGVGAFSFNTLYKLVWLKENHPQLLEQAHAWLFISSLINHRLTGEFTTDITMAGTSQMLDIQQRDFSPEILQATGL 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 204 PEHLFGEIILPGTIRGTLKEDIARETGLGT-VDVIAVGsHDTASAVAAVPAVENPiAFLSSGTWSLLGVEVDEPILTEEA 282
Cdd:PRK10331 201 SRRLFPRLVEAGEQIGTLQPSAAALLGLPVgIPVISAG-HDTQFALFGSGAGQNQ-PVLSSGTWEILMVRSAQVDTSLLS 278
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 283 RKAQFTNE-----GGVDGKIRFLQNITGLWILQRLmseWKAcgeEQNYDIIIpqaAEAQiaTIIPVDDATFMNPENMENA 357
Cdd:PRK10331 279 QYAGSTCEldsqsGLYNPGMQWLASGVLEWVRKLF---WTA---ETPYQTMI---EEAR--AIPPGADGVKMQCDLLACQ 347
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 358 LIHYCrhhALQVPKNKAETVRCVLQSLAFKYRQAVEQLnhclpSPIRQLN-----IIGGGSQNQLLNQLTADELGIPVYA 432
Cdd:PRK10331 348 NAGWQ---GVTLNTTRGHFYRAALEGLTAQLKRNLQVL-----EKIGHFKasellLVGGGSRNALWNQIKANMLDIPIKV 419
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1697055883 433 GPV-EATAMGNILTQAMAKGEIADLRELREIVTRSVtpQVYYP 474
Cdd:PRK10331 420 LDDaETTVAGAAMFGWYGVGEFSSPEQARAQMKYQY--RYFYP 460
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
51-444 |
4.05e-38 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 143.09 E-value: 4.05e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 51 YWDfpALFEDMKTGLKLAAQKGYAVKSIGIDTWGVDFGLIDKHGNLLGNPVCYRDARtegipeevfkllderqhyadtgi 130
Cdd:cd00366 48 WWQ--AVVEAIREVLAKAGIDPSDIAAIGISGQMPGVVLVDADGNPLRPAIIWLDRR----------------------- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 131 qvmaintlfqlysmkqhqdaqlevaRQLLFMPDLFSYFLTGVANNEYCIASTSELLDAQSRNWSVDTIRALGLPEHLFGE 210
Cdd:cd00366 103 -------------------------AKFLQPNDYIVFRLTGEFAIDYSNASGTGLYDIKTGDWSEELLDALGIPREKLPP 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 211 IILPGTIRGTLKEDIARETGL--GTvdVIAVGSHDTASAVAAVPAVENPIAFLSSGTWSLLGVEVDEPILTEEArkaqFT 288
Cdd:cd00366 158 IVESGEVVGRVTPEAAEETGLpaGT--PVVAGGGDTAAAALGAGVVEPGDAVDSTGTSSVLSVCTDEPVPPDPR----LL 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 289 NEGGV-DGKIRFLQNI--TGL---WILQRLMSEWKACGEEQNYDiiipqaaeAQIATIIPVDDATFMNPENM-ENALIHY 361
Cdd:cd00366 232 NRCHVvPGLWLLEGAIntGGAslrWFRDEFGEEEDSDAEYEGLD--------ELAAEVPPGSDGLIFLPYLSgERSPIWD 303
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 362 CRHHA----LQVPKNKAETVRCVLQSLAFKYRQAVEQLNHCLPSpIRQLNIIGGGSQNQLLNQLTADELGIPVYAGPV-E 436
Cdd:cd00366 304 PAARGvffgLTLSHTRAHLIRAVLEGVAYALRDNLEILEELGVK-IKEIRVTGGGAKSRLWNQIKADVLGVPVVVPEVaE 382
|
....*...
gi 1697055883 437 ATAMGNIL 444
Cdd:cd00366 383 GAALGAAI 390
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
51-469 |
3.66e-37 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 142.28 E-value: 3.66e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 51 YWDfpALFEDMKTGLKLAAQKGYAVKSIGIDTWGVDFGLIDKHGNLLGNPVCYRDARTEGIPEEVFKLLDERQHYADTGI 130
Cdd:COG1070 49 WWE--AVVEAIRELLAKAGVDPEEIAAIGVSGQMHGLVLLDADGEPLRPAILWNDTRAAAEAAELREELGEEALYEITGN 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 131 QVMAINTLFQLYSMKQHQDAQLEVARQLLFMPDLFSYFLTGVANNEYCIASTSELLDAQSRNWSVDTIRALGLPEHLFGE 210
Cdd:COG1070 127 PLHPGFTAPKLLWLKENEPEIFARIAKVLLPKDYLRYRLTGEFVTDYSDASGTGLLDVRTRDWSDELLEALGIDRELLPE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 211 IILPGTIRGTLKEDIARETGL--------GTVDV----IAVGSHDTAsavaavpavenpIAFLSSGTWSLLGVEVDEPIL 278
Cdd:COG1070 207 LVPPGEVAGTLTAEAAAETGLpagtpvvaGAGDNaaaaLGAGAVEPG------------DAAVSLGTSGVVFVVSDKPLP 274
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 279 TEEARKAQFTneGGVDGkiRFLQNI---TGLWILQRLMSEWkACGEEQNYDIIIPQAAEAQIA----TIIPvddatFMN- 350
Cdd:COG1070 275 DPEGRVHTFC--HAVPG--RWLPMGatnNGGSALRWFRDLF-ADGELDDYEELNALAAEVPPGadglLFLP-----YLSg 344
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 351 ---PENMENA---LIHYCRHHalqvpkNKAETVRCVLQSLAFKYRQAVEQLNHCLPsPIRQLNIIGGGSQNQLLNQLTAD 424
Cdd:COG1070 345 ertPHWDPNArgaFFGLTLSH------TRAHLARAVLEGVAFALRDGLEALEEAGV-KIDRIRATGGGARSPLWRQILAD 417
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1697055883 425 ELGIPVYAGPV-EATAMGNILTQAMAKGEIADLRELRE---IVTRSVTP 469
Cdd:COG1070 418 VLGRPVEVPEAeEGGALGAALLAAVGLGLYDDLEEAAAamvRVGETIEP 466
|
|
| FGGY_C |
pfam02782 |
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease ... |
259-449 |
2.74e-32 |
|
FGGY family of carbohydrate kinases, C-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the N-terminal domain.
Pssm-ID: 426979 [Multi-domain] Cd Length: 197 Bit Score: 122.05 E-value: 2.74e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 259 AFLSSGTWSLLGVEVDEPILTEEARKAQFTNE-----GGVDGKIRFLQNITGlWILQrlmsEWKACGEEQNYDIIIPQAA 333
Cdd:pfam02782 1 LAISAGTSSFVLVETPEPVLSVHGVWGPYTNEmlpgyWGLEGGQSAAGSLLA-WLLQ----FHGLREELRDAGNVESLAE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 334 EAQIAT-------IIPVDDATFMNPENMENALIHYcrhHALQVPKNKAETVRCVLQSLAFKYRQAVEQLNHCLPSPIRQL 406
Cdd:pfam02782 76 LAALAAvapagglLFYPDFSGNRAPGADPGARGSI---TGLSSPTTLAHLYRAILESLALQLRQILEALTKQEGHPIDTI 152
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1697055883 407 NIIGGGSQNQLLNQLTADELGIPVY-AGPVEATAMGNILTQAMA 449
Cdd:pfam02782 153 HVSGGGSRNPLLLQLLADALGLPVVvPGPDEATALGAALLAAVA 196
|
|
| ASKHA_NBD_FGGY_YoaC-like |
cd07798 |
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; ... |
9-441 |
5.95e-32 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis sugar kinase YoaC and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to Bacillus subtilis sugar kinase YoaC. It is part of the yoaDCB operon and induced by sulfate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466804 [Multi-domain] Cd Length: 448 Bit Score: 126.95 E-value: 5.95e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 9 YLAADFGGGSGR--IIAGFLHHGKLELEEvyrfcNRQVKLGNH---IYWD----FPALFEDMKTGLKLAAQKGYAVKSIG 79
Cdd:cd07798 2 YLVIDIGTGGGRcaLVDSEGKIVAIAYRE-----WEYYTDDDYpdaKEFDpeelWEKICEAIREALKKAGISPEDISAVS 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 80 IDTWGVDFGLIDKHGN-LLGNPvcYRDARteGIpEEVFKLLDERQH--YADTGIQVMAINTLFQLYSMKQHQDAQLEVAR 156
Cdd:cd07798 77 STSQREGIVFLDKDGReLYAGP--NIDAR--GV-EEAAEIDDEFGEeiYTTTGHWPTELFPAARLLWFKENRPEIFERIA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 157 QLLFMPDLFSYFLTGVANNEYCIASTSELLDAQSRNWSVDTIRALGLPEHLFGEIILPGTIRGTLKEDIARETGL--GTv 234
Cdd:cd07798 152 TVLSISDWIGYRLTGELVSEPSQASETQLFDIKKREWSQELLEALGLPPEILPEIVPSGTVLGTVSEEAARELGLpeGT- 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 235 dVIAVGSHDTASAVAAVPAVENPIAFLSSGTWSLLGVEVDEPILTEEARkaQFTNEGGVDGKIRFLQN--ITGL---WIL 309
Cdd:cd07798 231 -PVVVGGADTQCALLGSGAIEPGDIGIVAGTTTPVQMVTDEPIIDPERR--LWTGCHLVPGKWVLESNagVTGLnyqWLK 307
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 310 QRLMsewkaCGEEQNYDIIipqaaEAQIATIIPVDDAT--FMNPENMENALIHYCRH-HALQVP-----KNKAETVRCVL 381
Cdd:cd07798 308 ELLY-----GDPEDSYEVL-----EEEASEIPPGANGVlaFLGPQIFDARLSGLKNGgFLFPTPlsaseLTRGDFARAIL 377
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1697055883 382 QSLAFKYRQAVEQLNHCLPSPIRQLNIIGGGSQNQLLNQLTADELGIPVY-AGPVEATAMG 441
Cdd:cd07798 378 ENIAFAIRANLEQLEEVSGREIPYIILCGGGSRSALLCQILADVLGKPVLvPEGREASALG 438
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
89-451 |
9.87e-32 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 126.51 E-value: 9.87e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 89 LIDKHGNLLGNPVCYRDARTEGIPEEVFKLLDERQHYADTGIQVMAINTLFQLYSMKQHQDAQLEVARQLLFMPDLFSYF 168
Cdd:cd07802 84 LVDKDGKPVRNAILSNDSRAADIVDRWEEDGTLEKVYPLTGQPLWPGQPVALLRWLKENEPERYDRIRTVLFCKDWIRYR 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 169 LTGVANNEYCIASTSeLLDAQSRNWSVDTIRALGLPE--HLFGEIILPGTIRGTLKEDIARETGL--GT-VdviAVGSHD 243
Cdd:cd07802 164 LTGEISTDYTDAGSS-LLDLDTGEYDDELLDLLGIEElkDKLPPLVPSTEIAGRVTAEAAALTGLpeGTpV---AAGAFD 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 244 TASAVAAVPAVENPIAFLSSGTWSLLGVEVDEPILTEEARKAQFTNEGGvdgkiRFLQNITGL-------WILQRLMSEW 316
Cdd:cd07802 240 VVASALGAGAVDEGQLCVILGTWSINEVVTDEPVVPDSVGSNSLHADPG-----LYLIVEASPtsasnldWFLDTLLGEE 314
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 317 KACGEEqNYDIIipqaaEAQIATIIPVDDAT----FMNPENME-NAlihycR--------HHalqvpkNKAETVRCVLQS 383
Cdd:cd07802 315 KEAGGS-DYDEL-----DELIAAVPPGSSGViflpYLYGSGANpNA-----RggffgltaWH------TRAHLLRAVYEG 377
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 384 LAFKYRQAVEQL-NHCLPSPIRqlnIIGGGSQNQLLNQLTADELGIPVYAGPV-EATAMGNILTQAMAKG 451
Cdd:cd07802 378 IAFSHRDHLERLlVARKPETIR---LTGGGARSPVWAQIFADVLGLPVEVPDGeELGALGAAICAAVAAG 444
|
|
| ASKHA_NBD_FGGY_CvXK-like |
cd07805 |
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and ... |
89-474 |
1.83e-29 |
|
nucleotide-binding domain (NBD) of Chromobacterium violaceum xylulose kinase (CvXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Chromobacterium violaceum xylulose kinase (CvXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466807 [Multi-domain] Cd Length: 485 Bit Score: 120.32 E-value: 1.83e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 89 LIDKHGNLLGNPVCYRDARTEGIPEEVFKLLDERQHYADTGIQVM-AINTLFQLYSMKQHQDAQLEVARQLLFMPDLFSY 167
Cdd:cd07805 84 PVDKDGNPLRNAIIWSDTRAAEEAEEIAGGLGGIEGYRLGGGNPPsGKDPLAKILWLKENEPEIYAKTHKFLDAKDYLNF 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 168 FLTGVANNEYCIASTSELLDAQSRNWSVDTIRALGLPEHLFGEIILPGTIRGTLKEDIARETGL--------GTVDV--I 237
Cdd:cd07805 164 RLTGRAATDPSTASTTGLMDLRKRRWSEELLRAAGIDPDKLPELVPSTEVVGELTPEAAAELGLpagtpvvgGGGDAaaA 243
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 238 AVGShdtasavaavPAVENPIAFLSSGTWSLLGVEVDEPILTEEARKAQFTneGGVDGKIrflqNITGL---------WI 308
Cdd:cd07805 244 ALGA----------GAVEEGDAHIYLGTSGWVAAHVPKPKTDPDHGIFTLA--SADPGRY----LLAAEqetaggaleWA 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 309 LQRLMSEwkACGEEQNYDIIIPQAAEAQIAT--II----------PVDDatfmnpENMENALIHYCRHHalqvpkNKAET 376
Cdd:cd07805 308 RDNLGGD--EDLGADDYELLDELAAEAPPGSngLLflpwlngersPVED------PNARGAFIGLSLEH------TRADL 373
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 377 VRCVLQSLAFKYRQAVEQLNHcLPSPIRQLNIIGGGSQNQLLNQLTADELGIPVY--AGPVEATAMGNILTQAMAKGEIA 454
Cdd:cd07805 374 ARAVLEGVAFNLRWLLEALEK-LTRKIDELRLVGGGARSDLWCQILADVLGRPVEvpENPQEAGALGAALLAAVGLGLLK 452
|
410 420
....*....|....*....|
gi 1697055883 455 DLRELREIVTRSvtpQVYYP 474
Cdd:cd07805 453 SFDEAKALVKVE---KVFEP 469
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
56-476 |
1.65e-25 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466808 [Multi-domain] Cd Length: 482 Bit Score: 108.78 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 56 ALFEDMKTGLKLAAQKGYAVKSIGIDtwgvdfG------LIDKHGNLLGNPVCYRDARTEGIPEEVFKLLDERQHYAdTG 129
Cdd:cd07808 51 ATKEALRELLAKAGISPSDIAAIGLT------GqmhglvLLDKNGRPLRPAILWNDQRSAAECEELEARLGDEILII-TG 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 130 IQVMAINTLFQLYSMKQHQDAQLEVARQLLFMPDLFSYFLTGVANNEYCIASTSELLDAQSRNWSVDTIRALGLPEHLFG 209
Cdd:cd07808 124 NPPLPGFTLPKLLWLKENEPEIFARIRKILLPKDYLRYRLTGELATDPSDASGTLLFDVEKREWSEELLEALGLDPSILP 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 210 EIILPGTIRGTLKEDIARETGL--GTVdVIAvGSHDTASAVAAVPAVENPIAFLSSGTWSLLGVEVDEPILTEEARkaqf 287
Cdd:cd07808 204 PIVESTEIVGTLTPEAAEELGLpeGTP-VVA-GAGDNAAAALGAGVVEPGDALISLGTSGVVFAPTDKPVPDPKGR---- 277
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 288 tneggvdgkirfLQN----ITGLWILQRLMS------EW---KACGEEQNYDIIIPQAAEAQIATiipvDDATF------ 348
Cdd:cd07808 278 ------------LHTfphaVPGKWYAMGVTLsaglslRWlrdLFGPDRESFDELDAEAAKVPPGS----EGLLFlpylsg 341
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 349 -----MNPeNMENALIHYCRHHalqvpkNKAETVRCVLQSLAFKYRQAVEQLNHCLPsPIRQLNIIGGGSQNQLLNQLTA 423
Cdd:cd07808 342 ertpyWDP-NARGSFFGLSLSH------TRAHLARAVLEGVAFSLRDSLEVLKELGI-KVKEIRLIGGGAKSPLWRQILA 413
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1697055883 424 DELGIPVYAGPV-EATAMGNILTQAMAKGEIADLRELREIVTRsvTPQVYYPKK 476
Cdd:cd07808 414 DVLGVPVVVPAEeEGSAYGAALLAAVGAGVFDDLEEAAAACIK--IEKTIEPDP 465
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
49-474 |
4.03e-24 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466798 [Multi-domain] Cd Length: 433 Bit Score: 104.14 E-value: 4.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 49 HIYWDfpALFEDMKTGLKLAAQKGYAVKSIGIDTWGVDFGLIDKHGNLLGNPVCYRDARTegipeevfkllderqhyadt 128
Cdd:cd07779 46 DDWWD--ALCEALKEAVAKAGVDPEDIAAIGLTSQRSTFVPVDEDGRPLRPAISWQDKRT-------------------- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 129 giqvmaintlfqlysmkqhqdaqlevaRQLLFMPDLFSYFLTGVANNEYCIASTSELLDAQSRNWSVDTIRALGLPEHLF 208
Cdd:cd07779 104 ---------------------------AKFLTVQDYLLYRLTGEFVTDTTSASRTGLPDIRTRDWSDDLLDAFGIDRDKL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 209 GEIILPGTIRGTLKEDIARETGLGT-VDVIAvGSHDTASAVAAVPAVENPIAFLSSGTWSLLGVEVDEPILTEEAR---- 283
Cdd:cd07779 157 PELVPPGTVIGTLTKEAAEETGLPEgTPVVA-GGGDQQCAALGAGVLEPGTASLSLGTAAVVIAVSDKPVEDPERRipcn 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 284 ----KAQFTNEGGVdgkirflqnITGLWILQRLMSE------WKACGEEQNYDIIIPQAAEaqiatiIPV--DDATF--- 348
Cdd:cd07779 236 psavPGKWVLEGSI---------NTGGSAVRWFRDEfgqdevAEKELGVSPYELLNEEAAK------SPPgsDGLLFlpy 300
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 349 ----MNPENMENA--------LIHycrhhalqvpkNKAETVRCVLQSLAFKYRQAVEQLNHCLPsPIRQLNIIGGGSQNQ 416
Cdd:cd07779 301 lagaGTPYWNPEArgafigltLSH-----------TRAHLARAILEGIAFELRDNLEAMEKAGV-PIEEIRVSGGGSKSD 368
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1697055883 417 LLNQLTADELGIPVYAGPV-EATAMGNILTQAMAKGEIADLRELREIVTRsvTPQVYYP 474
Cdd:cd07779 369 LWNQIIADVFGRPVERPETsEATALGAAILAAVGAGIYPDFEEAVKAMVR--VTDTFEP 425
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
53-469 |
1.20e-23 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 103.40 E-value: 1.20e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 53 DFPALFEDMKTGLK--LAAQKGYAVKSIGIDT-WgvdFGLI--DKHGNLLGNPVCYRDARTEGIPEEVFKLLDERQHYAD 127
Cdd:cd07770 44 DPEEILEAVLEALKevLAKLGGGEVDAIGFSSaM---HSLLgvDEDGEPLTPVITWADTRAAEEAERLRKEGDGSELYRR 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 128 TGIQVMAINTLFQLYSMKQHQDAQLEVARQLLFMPDLFSYFLTGVANNEYCIASTSELLDAQSRNWSVDTIRALGLPEHL 207
Cdd:cd07770 121 TGCPIHPMYPLAKLLWLKEERPELFAKAAKFVSIKEYLLYRLTGELVTDYSTASGTGLLNIHTLDWDEEALELLGIDEEQ 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 208 FGEIILPGTIRGTLKEDIARETGL--GTVDVIA--------VGSHDTasavaavpaVENPIAfLSSGTWSLLGVEVDEPI 277
Cdd:cd07770 201 LPELVDPTEVLPGLKPEFAERLGLlaGTPVVLGasdgalanLGSGAL---------DPGRAA-LTVGTSGAIRVVSDRPV 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 278 LTEEARkaQF--------------TNEGGVdgkirFLQnitglWILQRLmsewkaCGEEQNYDIIIPQAAEAQIA----T 339
Cdd:cd07770 271 LDPPGR--LWcyrldenrwlvggaINNGGN-----VLD-----WLRDTL------LLSGDDYEELDKLAEAVPPGshglI 332
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 340 IIPvddatFMNPE-------NMENALIHYCRHHalqvpkNKAETVRCVLQSLAFKYRQAVEQLNHCLPsPIRQLNIIGGG 412
Cdd:cd07770 333 FLP-----YLAGErapgwnpDARGAFFGLTLNH------TRADILRAVLEGVAFNLKSIYEALEELAG-PVKEIRASGGF 400
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*....
gi 1697055883 413 SQNQLLNQLTADELGIPVYAGPV-EATAMGNILTQAMAKGEIADLRELREI-VTRSVTP 469
Cdd:cd07770 401 LRSPLWLQILADVLGRPVLVPEEeEASALGAALLALEALGLISSLEADELVkIGKVVEP 459
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
9-441 |
3.08e-21 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466801 [Multi-domain] Cd Length: 429 Bit Score: 95.75 E-value: 3.08e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 9 YLAADFGGGSGRIIA-----GFLHHGKLELEEVYRFCNRQVKLGNHiYWDfpALFEDMKtglKLAAQ-KGYAVKSIGID- 81
Cdd:cd07783 2 FLGIDLGTSGVRAVVvdedgTVLASASEPYPTSRPGPGWVEQDPED-WWE--ALRSLLR---ELPAElRPRRVVAIAVDg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 82 TWGVDFgLIDKHGNLLGNPVCYRDARTEGIPEEVFKLLDErqHYADTGIQVMAINTLFQLYSMKQHQDAQLEVARQLLFM 161
Cdd:cd07783 76 TSGTLV-LVDREGEPLRPAIMYNDARAVAEAEELAEAAGA--VAPRTGLAVSPSSSLAKLLWLKRHEPEVLAKTAKFLHQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 162 PDLFSYFLTGVA-----NNeyciASTSeLLDAQSRNWSVDTIRALGLPEHLFGEIILPGTIRGTLKEDIARETGL----- 231
Cdd:cd07783 153 ADWLAGRLTGDRgvtdyNN----ALKL-GYDPETGRWPSWLLALLGIPPDLLPRVVAPGTVIGTLTAEAAEELGLpagtp 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 232 ---GTVD----VIAVGShdtasavaavpaVENPIAFLSSGTWSLLGVEVDEPILTEEARkaqFTNEGGVDGkiRFL---- 300
Cdd:cd07783 228 vvaGTTDsiaaFLASGA------------VRPGDAVTSLGTTLVLKLLSDKRVPDPGGG---VYSHRHGDG--YWLvgga 290
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 301 QNITGLWILQRLmsewkacgEEQNYDIIIPQAAEAQIATII-----------PVDDAtfmnpeNMENALihycrhhaLQV 369
Cdd:cd07783 291 SNTGGAVLRWFF--------SDDELAELSAQADPPGPSGLIyyplplrgerfPFWDP------DARGFL--------LPR 348
|
410 420 430 440 450 460 470
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1697055883 370 PKNKAETVRCVLQSLAFKYRQAVEQLNHCLPSPIRQLNIIGGGSQNQLLNQLTADELGIPVYAGPVEATAMG 441
Cdd:cd07783 349 PHDRAEFLRALLEGIAFIERLGYERLEELGAPPVEEVRTAGGGARNDLWNQIRADVLGVPVVIAEEEEAALG 420
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
9-244 |
1.15e-20 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 90.86 E-value: 1.15e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 9 YLAADFGGGSGRIIAgFLHHGKLELEEVYRFCNRQVKLGNHIyWD----FPALFEDMKTGLKLAAQKGYAVKSIGIDTWG 84
Cdd:pfam00370 2 YLGIDCGTTSTKAIL-FNEQGKIIAVAQLENPQITPHPGWAE-QDpdeiWQAVAQCIAKTLSQLGISLKQIKGIGISNQG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 85 VDFGLIDKHGNLLGNPVCYRDARTEGIPEEVFKLLDERQHYADTGIQVMAINTLFQLYSMKQHQDAQLEVARQLLFMPDL 164
Cdd:pfam00370 80 HGTVLLDKNDKPLYNAILWKDRRTAEIVENLKEEGNNQKLYEITGLPIWPGFTLSKLRWIKENEPEVFEKIHKFLTIHDY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 165 FSYFLTGVANNEYCIASTSELLDAQSRNWSVDTIRALGLPEHLFGEIILPGTIRGTLKEDIARETGLGTVDVIAVGSHDT 244
Cdd:pfam00370 160 LRWRLTGVFVTDHTNASRSMMFNIHKLDWDPELLAALGIPRDHLPPLVESSEIYGELNPELAAMWGLDEGVPVVGGGGDQ 239
|
|
| ASKHA_NBD_FGGY_AI-2K |
cd07775 |
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; ... |
105-476 |
2.66e-19 |
|
nucleotide-binding domain (NBD) of autoinducer-2 kinase (AI-2 kinase) and similar proteins; AI-2 kinase (EC 2.7.1.189), also known as LsrK, catalyzes the phosphorylation of autoinducer-2 (AI-2) to phospho-AI-2, which subsequently inactivates the transcriptional regulator LsrR and leads to the transcription of the lsr operon. It phosphorylates the ring-open form of (S)-4,5-dihydroxypentane-2,3-dione (DPD), which is the precursor to all AI-2 signaling molecules, at the C5 position. It is required for the regulation of the lsr operon and many other genes. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466794 [Multi-domain] Cd Length: 492 Bit Score: 90.47 E-value: 2.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 105 DARTEgipEEVFKLLD-----ERQHYADTGiQVMAINTLFQLYSMKQHQDAQLEVARQLLFMPDLFSYFLTGVANNEYCI 179
Cdd:cd07775 101 DARAA---EEVSELKElyntlEEEVYRISG-QTFALGAIPRLLWLKNNRPEIYRKAAKITMLSDWIAYKLSGELAVEPSN 176
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 180 ASTSELLDAQSRNWSVDTIRALGLPEHLFGEIILPGTIRGTLKEDIARETGLGTVDVIAVGSHDTASAVAAV-PAVENPI 258
Cdd:cd07775 177 GSTTGLFDLKTRDWDPEILEMAGLKADILPPVVESGTVIGKVTKEAAEETGLKEGTPVVVGGGDVQLGCLGLgVVRPGQT 256
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 259 AFLSSGTWSLLgVEVDEPILTEEAR--------KAQFTNEGgvdgkIRFLQNITGLWILQRLMSEWKACGEEQN---YDI 327
Cdd:cd07775 257 AVLGGSFWQQE-VNTAAPVTDPAMNirvnchviPDMWQAEG-----ISFFPGLVMRWFRDAFCAEEKEIAERLGidaYDL 330
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 328 IIPQAAEAQIAT--IIPVddatFMNPENMENalihyCRHHA-------LQVPK-NKAETVRCVLQSLAFKYRQAVEQLNH 397
Cdd:cd07775 331 LEEMAKDVPPGSygIMPI----FSDVMNYKN-----WRHAApsflnldIDPEKcNKATFFRAIMENAAIVSAGNLERIAE 401
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 398 CLPSPIRQLNIIGGGSQNQLLNQLTADELGIPVYAgPV--EATAMGNILTQAMAKGEIADLRELREIVTRsvTPQVYYPK 475
Cdd:cd07775 402 FSGIFPDSLVFAGGASKGKLWCQILADVLGLPVKV-PVvkEATALGAAIAAGVGAGIYSSLEEAVESLVK--WEREYLPN 478
|
.
gi 1697055883 476 K 476
Cdd:cd07775 479 P 479
|
|
| ASKHA_NBD_FGGY_BaEryA-like |
cd24121 |
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar ... |
74-430 |
1.26e-18 |
|
nucleotide-binding domain (NBD) of Brucella abortus erythritol kinase (BaEryA) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). It catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466971 [Multi-domain] Cd Length: 452 Bit Score: 88.07 E-value: 1.26e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 74 AVKSIGI----D-TWgvdfgLIDKHGNLLGNPVCYRDART---------EGIPEEVFKLlderqhyadTGIQVMAINTLF 139
Cdd:cd24121 69 RVAAIGVtgqgDgTW-----LVDEDGRPVRDAILWLDGRAadiverwqaDGIAEAVFEI---------TGTGLFPGSQAA 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 140 QLYSMKQHQDAQLEVARQLLFMPDLFSYFLTGVANNEYCIASTSeLLDAQSRNWSVDTIRALGLPE--HLFGEIILPGTI 217
Cdd:cd24121 135 QLAWLKENEPERLERARTALHCKDWLFYKLTGEIATDPSDASLT-FLDFRTRQYDDEVLDLLGLEElrHLLPPIRPGTEV 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 218 RGTLKEDIARETGL--------GTVDVI--AVGShdtasavaavPAVENPIAFLSSGTWSLLGVEVDEPILteEARKAQF 287
Cdd:cd24121 214 IGPLTPEAAAATGLpagtpvvlGPFDVVatALGS----------GAIEPGDACSILGTTGVHEVVVDEPDL--EPEGVGY 281
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 288 TNEGGVDGK-IRFLQNITGL----WILQRLMSEWKAcgEEQNYDIIIPQAAEAQIATIIPVDDATFMNP---ENMENA-- 357
Cdd:cd24121 282 TICLGVPGRwLRAMANMAGTpnldWFLRELGEVLKE--GAEPAGSDLFQDLEELAASSPPGAEGVLYHPylsPAGERApf 359
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 358 --------LIHYCRHHalqvpkNKAETVRCVLQSLAFKYRqaveqlnHC---LPSPIRQLNIIGGGSQNQLLNQLTADEL 426
Cdd:cd24121 360 vnpnaraqFTGLSLEH------TRADLLRAVYEGVALAMR-------DCyehMGEDPGELRLSGGGARSDTWCQILADAL 426
|
....
gi 1697055883 427 GIPV 430
Cdd:cd24121 427 GVPV 430
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
53-267 |
3.07e-14 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 74.22 E-value: 3.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 53 DFPALFEDMKTGLKLAAQKgYAVKSIGIDTWGVDFGLIDKHGNLLGNPVCYRDArtegIPEEVFKLLDE-RQHYADTG-- 129
Cdd:cd07772 43 DVEAIWEWLLDSLAELAKR-HRIDAINFTTHGATFALLDENGELALPVYDYEKP----IPDEINEAYYAeRGPFEETGsp 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 130 IQVMAINTLFQLYSMKQHQDAQLEVARQLLFMPDLFSYFLTGVANNEYCIAST-SELLDAQSRNWSvDTIRALGLpEHLF 208
Cdd:cd07772 118 PLPGGLNLGKQLYWLKREKPELFARAKTILPLPQYWAWRLTGKAASEITSLGChTDLWDFEKNEYS-SLVKKEGW-DKLF 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 209 GEIILPGTIRGTLKEDIARETGLGTVDVIAVGSHD-TASAVAAVPAVENPIAFLSSGTWS 267
Cdd:cd07772 196 PPLRKAWEVLGPLRPDLARRTGLPKDIPVGCGIHDsNAALLPYLAAGKEPFTLLSTGTWC 255
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
75-451 |
6.16e-12 |
|
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466806 [Multi-domain] Cd Length: 451 Bit Score: 67.17 E-value: 6.16e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 75 VKSIGIDTWGVDFGLIDKHGNLLGNPVCYRDARTEGIPEEVFKLLDERQHYADTGiqvMAINTLF---QLYSMKQHQDAQ 151
Cdd:cd07804 70 IAAIGVSGLVPALVPVDENGKPLRPAILYGDRRATEEIEWLNENIGEDRIFEITG---NPLDSQSvgpKLLWIKRNEPEV 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 152 LEVARQLLFMPDLFSYFLTGVANNEYCIAS-TSELLDAQSRNWSVDTIRALGLPEHLFGEIILPGTIRGTLKEDIARETG 230
Cdd:cd07804 147 FKKTRKFLGAYDYIVYKLTGEYVIDYSSAGnEGGLFDIRKRTWDEELLEALGIDPDLLPELVPSTEIVGEVTKEAAEETG 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 231 L--------GTVDVIA-------VGSHDTAsavaavpavenpIAFLSSGTWSLLGVEVDEPI---LTEEARKAQF----- 287
Cdd:cd07804 227 LaegtpvvaGTVDAAAsalsagvVEPGDLL------------LMLGTAGDIGVVTDKLPTDPrlwLDYHDIPGTYvlngg 294
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 288 -TNEGGVdgkIR-FLQNitglwILQRLMSEWKACGEEqNYDIIIPQAAEAQIAT----IIPVddatFM---NPENMENA- 357
Cdd:cd07804 295 mATSGSL---LRwFRDE-----FAGEEVEAEKSGGDS-AYDLLDEEAEKIPPGSdgliVLPY----FMgerTPIWDPDAr 361
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 358 -LIHYCR-HHalqvpkNKAETVRCVLQSLAFKYRQAVEQLNHCLPsPIRQLNIIGGGSQNQLLNQLTADELGIPVY--AG 433
Cdd:cd07804 362 gVIFGLTlSH------TRAHLYRALLEGVAYGLRHHLEVIREAGL-PIKRLVAVGGGAKSPLWRQIVADVTGVPQEyvKD 434
|
410
....*....|....*...
gi 1697055883 434 PVEAtAMGNILTQAMAKG 451
Cdd:cd07804 435 TVGA-SLGDAFLAGVGVG 451
|
|
| ASKHA_NBD_FGGY_BaXK-like |
cd07809 |
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and ... |
65-441 |
1.78e-11 |
|
nucleotide-binding domain (NBD) of Bifidobacterium adolescentis xylulose kinase (XK) and similar proteins; The subfamily includes a group of uncharacterized proteins with similarity to xylulose kinases (XKs) from Bifidobacterium adolescentis, Streptomyces coelicolor, Actinoplanes missouriensis and Haemophilus influenzae. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466809 [Multi-domain] Cd Length: 443 Bit Score: 66.03 E-value: 1.78e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 65 LKLAAQKGYAVKSIGIDTWGVDFGLIDKHGNLLGNPVCYRDARTEGIPEEVFKLLDERQhYADTGIQVMAINTLFQLYSM 144
Cdd:cd07809 61 LKDAGAELRDVAAIGISGQMHGLVALDADGKVLRPAKLWCDTRTAPEAEELTEALGGKK-CLLVGLNIPARFTASKLLWL 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 145 KQHQDAQLEVARQLLFMPDLFSYFLTGVANNEYCIASTSELLDAQSRNWS---VDTIRALGLPEHLFGEIILPGTIRGTL 221
Cdd:cd07809 140 KENEPEHYARIAKILLPHDYLNWKLTGEKVTGLGDASGTFPIDPRTRDYDaelLAAIDPSRDLRDLLPEVLPAGEVAGRL 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 222 KEDIARETGLGTVDVIAVGSHDtasavaavpaveNPIAFLS---------------SGTwsLLGVeVDEPILTEEARKAQ 286
Cdd:cd07809 220 TPEGAEELGLPAGIPVAPGEGD------------NMTGALGtgvvnpgtvavslgtSGT--AYGV-SDKPVSDPHGRVAT 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 287 FTnegGVDGkiRFLQNITGLWILQRLMsEWKACGEEQNYDIIIPQAAEAQIA----TIIPvddatFMNPENMEN-----A 357
Cdd:cd07809 285 FC---DSTG--GMLPLINTTNCLTAWT-ELFRELLGVSYEELDELAAQAPPGagglLLLP-----FLNGERTPNlphgrA 353
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 358 LIHYCRHHALqvpkNKAETVRCVLQSLAFKYRQAVEQLnHCLPSPIRQLNIIGGGSQNQLLNQLTADELGIPVY-AGPVE 436
Cdd:cd07809 354 SLVGLTLSNF----TRANLARAALEGATFGLRYGLDIL-RELGVEIDEIRLIGGGSKSPVWRQILADVFGVPVVvPETGE 428
|
....*
gi 1697055883 437 ATAMG 441
Cdd:cd07809 429 GGALG 433
|
|
| ASKHA_NBD_FGGY_GK1-3-like |
cd07792 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; ... |
372-475 |
3.47e-09 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 1-3 (GK1-3) and similar proteins; This subfamily contains metazoan glycerol kinases (GKs), coded by X chromosome-linked GK genes, and glycerol kinase (GK)-like proteins, coded by autosomal testis-specific GK-like genes (GK-like genes, GK2 and GK3). Sequence comparison shows that metazoan GKs and GK-like proteins in this family are closely related to the bacterial GKs (EC 2.7.1.30), which catalyze the Mg-ATP dependent phosphorylation of glycerol to yield glycerol 3-phosphate (G3P). The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466802 [Multi-domain] Cd Length: 499 Bit Score: 58.69 E-value: 3.47e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 372 NKAETVRCVLQSLAFKYRQAVEQLNHCLPSPIRQLNIIGGGSQNQLLNQLTADELGIPVYAGP-VEATAMGNILTQAMAK 450
Cdd:cd07792 377 TKAHIARAALEAVCFQTREILDAMNKDSGIPLTSLRVDGGMTKNNLLMQIQADILGIPVERPSmVETTALGAAIAAGLAV 456
|
90 100
....*....|....*....|....*
gi 1697055883 451 GEIADLRELREIVTRSVTpqVYYPK 475
Cdd:cd07792 457 GVWKSLDELKSLNEGGRT--VFEPQ 479
|
|
| PRK10939 |
PRK10939 |
autoinducer-2 (AI-2) kinase; Provisional |
105-451 |
1.15e-08 |
|
autoinducer-2 (AI-2) kinase; Provisional
Pssm-ID: 182853 [Multi-domain] Cd Length: 520 Bit Score: 57.32 E-value: 1.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 105 DARTEgipEEVFKLLD-----ERQHYADTGiQVMAINTLFQLYSMKQHQDAQLEVARQLLFMPDLFSYFLTGVANNEYCI 179
Cdd:PRK10939 104 DARAS---REVSELKElhnnfEEEVYRCSG-QTLALGALPRLLWLAHHRPDIYRQAHTITMISDWIAYMLSGELAVDPSN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 180 ASTSELLDAQSRNWSVDTIRALGLPEHLFGEIILPGTIRGTLKEDIARETGL--GTvDVIAVGSHDTASAVAAVPAVENP 257
Cdd:PRK10939 180 AGTTGLLDLVTRDWDPALLEMAGLRADILPPVKETGTVLGHVTAKAAAETGLraGT-PVVMGGGDVQLGCLGLGVVRPGQ 258
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 258 IAFLSSGTWSLLgVEVDEPILTEEARKAqfTNEGGVDG-----KIRFLQNITGLWILQRLMSEWKACGEEQN---YDIII 329
Cdd:PRK10939 259 TAVLGGTFWQQV-VNLPAPVTDPNMNIR--INPHVIPGmvqaeSISFFTGLTMRWFRDAFCAEEKLLAERLGidaYSLLE 335
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 330 PQAAEAQIAT--IIPVddatFMNPenmenalIHYCR-HHA------LQV-PK--NKAETVRCVLQSLAFKYR---QAVEQ 394
Cdd:PRK10939 336 EMASRVPVGShgIIPI----FSDV-------MRFKSwYHAapsfinLSIdPEkcNKATLFRALEENAAIVSAcnlQQIAA 404
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1697055883 395 LNHCLPSPIRqlnIIGGGSQNQLLNQLTADELGIPVYAgPV--EATAMGNiltqAMAKG 451
Cdd:PRK10939 405 FSGVFPSSLV---FAGGGSKGKLWSQILADVTGLPVKV-PVvkEATALGC----AIAAG 455
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
66-441 |
4.14e-07 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 52.22 E-value: 4.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 66 KLAAQKGYAVKSIGIDTW--GvdFGLIDKHGNLLGNPVCYRDAR-TEGIPEEVFKLLDERQHyaDTGIQV---MAINTLF 139
Cdd:cd07777 61 ELPREYLSDVTGIGITGQmhG--IVLWDEDGNPVSPLITWQDQRcSEEFLGGLSTYGEELLP--KSGMRLkpgYGLATLF 136
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 140 QlysMKQHQDAQLEVARqLLFMPDLFSYFLTGvaNNEYCIASTSE----LLDAQSRNWSVDTIRALGLPEHLFGEIILPG 215
Cdd:cd07777 137 W---LLRNGPLPSKADR-AGTIGDYIVARLTG--LPKPVMHPTNAaswgLFDLETGTWNKDLLEALGLPVILLPEIVPSG 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 216 TIRGTLKEDIARetglgTVDV-IAVGshDtasavaavpaveNPIAFLSS------------GTWSLLGVEVDEPILTE-- 280
Cdd:cd07777 211 EIVGTLSSALPK-----GIPVyVALG--D------------NQASVLGSglneendavlniGTGAQLSFLTPKFELSGsv 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 281 EARKaqFTNEggvdgkiRFLQNITGL-------WI---LQRLMSEwkACG---EEQNYDIIIPQAAEAQIATIIpVDdaT 347
Cdd:cd07777 272 EIRP--FFDG-------RYLLVAASLpggralaVLvdfLREWLRE--LGGslsDDEIWEKLDELAESEESSDLS-VD--P 337
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 348 FMNPENMENAL---IHYCRHHALQVpknkAETVRCVLQSLAFKYRQAVEQLNhCLPSPIRQLNIIGGGSQ-NQLLNQLTA 423
Cdd:cd07777 338 TFFGERHDPEGrgsITNIGESNFTL----GNLFRALCRGIAENLHEMLPRLD-LDLSGIERIVGSGGALRkNPVLRRIIE 412
|
410
....*....|....*....
gi 1697055883 424 DELGIPV-YAGPVEATAMG 441
Cdd:cd07777 413 KRFGLPVvLSEGSEEAAVG 431
|
|
| ASKHA_NBD_FGGY_GK |
cd07769 |
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), ... |
372-441 |
5.99e-07 |
|
nucleotide-binding domain (NBD) of glycerol kinase (GK) and similar proteins; GK (EC 2.7.1.30), also called ATP:glycerol 3-phosphotransferase, or glycerokinase, is a key enzyme in the regulation of glycerol uptake and metabolism. It catalyzes the Mg-ATP-dependent phosphorylation of glycerol to yield sn-glycerol 3-phosphate. It also catalyzes the phosphorylation of dihydroxyacetone, L-glyceraldehyde and D-glyceraldehyde. The subfamily includes GKs and GK-like proteins from all three kingdoms of living organisms. Metazoan GKs, coded by X chromosome-linked GK genes, and GK-like proteins, coded by autosomal testis-specific GK-like genes GK2, GK3 and Gykl1 (in mouse) are closely related to the bacterial GKs. The metazoan GKs do have GK enzymatic activity. However, the GK-like metazoan proteins do not exhibit GK activity and their biological functions are not yet clear. Some of them lack important functional residues involved in the binding of ADP and Mg2+, which may result in the loss of GK catalytic function. Others that have conserved catalytic residues have lost their GK activity as well; the reason remains unclear. It has been suggested the conserved catalytic residues might facilitate them performing a distinct function. Under different conditions, GKs from different species may exist in different oligomeric states. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466789 [Multi-domain] Cd Length: 486 Bit Score: 51.70 E-value: 5.99e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1697055883 372 NKAETVRCVLQSLAFKYRQAVEQLNHCLPSPIRQLNIIGGGSQNQLLNQLTADELGIPVyAGPV--EATAMG 441
Cdd:cd07769 367 TKAHIVRAALESIAYQTRDVLEAMEKDSGIKLKELRVDGGATANNFLMQFQADILGVPV-VRPKvaETTALG 437
|
|
| ASKHA_NBD_FGGY_GK5-like |
cd07793 |
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The ... |
373-475 |
6.41e-07 |
|
nucleotide-binding domain (NBD) of metazoan glycerol kinase 5 (GK5) and similar proteins; The subfamily corresponds to a group of metazoan putative glycerol kinases (GK), which may be coded by the GK-like gene, GK5. Sequence comparison shows members of this group are homologs of bacterial GKs, and they retain all functionally important residues. However, GK-like proteins in this family do not have detectable GK activity. The reason remains unclear. It has been suggested that the conserved catalytic residues might facilitate them performing a distinct function. GK5 is a skin-specific kinase expressed predominantly in sebaceous glands. It can form a complex with the sterol regulatory element-binding proteins (SREBPs) through their C-terminal regulatory domains, inhibiting SREBP processing and activation. GK5 also promotes gefitinib resistance by inhibiting apoptosis and cell cycle arrest. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466803 [Multi-domain] Cd Length: 501 Bit Score: 51.79 E-value: 6.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 373 KAETVRCVLQSLAFKYRQAVEQLNHCLPSPIRQLNIIGGGSQNQLLNQLTADELGIPVYAGP-VEATAMGNILTQAMAKG 451
Cdd:cd07793 383 KAHLVRAILESIAFRVKQLLETMEKETSIKISSIRVDGGVSNNDFILQLIADLLGKPVERPKnTEMSALGAAFLAGLASG 462
|
90 100
....*....|....*....|....*..
gi 1697055883 452 ---EIADLRELReIVTRSVTPQVYYPK 475
Cdd:cd07793 463 iwkSKEELKKLR-KIEKIFEPKMDNEK 488
|
|
| FGGY_EcGK_like |
cd07786 |
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate ... |
372-470 |
4.71e-06 |
|
Escherichia coli glycerol kinase-like proteins; belongs to the FGGY family of carbohydrate kinases; This subgroup is composed of mostly bacterial and archaeal glycerol kinases (GK), including the well characterized proteins from Escherichia coli (EcGK), Thermococcus kodakaraensis (TkGK), and Enterococcus casseliflavus (EnGK). GKs contain two large domains separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. The high affinity ATP binding site of EcGK is created only by a substrate-induced conformational change, which is initiated by protein-protein interactions through complex formation with enzyme IIAGlc (also known as IIIGlc), the glucose-specific phosphocarrier protein of the phosphotransferase system (PTS). EcGK exists in a dimer-tetramer equilibrium. IIAGlc binds to both EcGK dimer and tetramer, and inhibits the uptake and subsequent metabolism of glycerol and maltose. Another well-known allosteric regulator of EcGK is fructose 1,6-bisphosphate (FBP), which binds to the EcGK tetramer and plays an essential role in the stabilization of the inactive tetrameric form. EcGK requires Mg2+ for its enzymatic activity. Members in this subgroup belong to the FGGY family of carbohydrate kinases
Pssm-ID: 198361 [Multi-domain] Cd Length: 486 Bit Score: 49.03 E-value: 4.71e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 372 NKAETVRCVLQSLAFKYRQAVEQLNHCLPSPIRQLNIIGGGSQNQLLNQLTADELGIPVyAGP--VEATAMGNILTQAMA 449
Cdd:cd07786 367 TRAHIARAALESIAYQTRDLLEAMEADSGIPLKELRVDGGASANDFLMQFQADILGVPV-ERPkvTETTALGAAYLAGLA 445
|
90 100
....*....|....*....|...
gi 1697055883 450 KGEIADLRELREI--VTRSVTPQ 470
Cdd:cd07786 446 VGLWKSLDELAKLwqVDRRFEPS 468
|
|
| PLN02295 |
PLN02295 |
glycerol kinase |
372-475 |
7.38e-06 |
|
glycerol kinase
Pssm-ID: 215166 [Multi-domain] Cd Length: 512 Bit Score: 48.16 E-value: 7.38e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 372 NKAETVRCVLQSLAFKYRQ--------AVEQLNHclpSPIRQLNIIGGGSQNQLLNQLTADELGIPVYAgP--VEATAMG 441
Cdd:PLN02295 377 NKAHIARAVLESMCFQVKDvldamrkdAGEEKSH---KGLFLLRVDGGATANNLLMQIQADLLGSPVVR-PadIETTALG 452
|
90 100 110
....*....|....*....|....*....|....*.
gi 1697055883 442 niltQAMAKGEIADLRELREIVTRSV--TPQVYYPK 475
Cdd:PLN02295 453 ----AAYAAGLAVGLWTEEEIFASEKwkNTTTFRPK 484
|
|
| PRK15027 |
PRK15027 |
xylulokinase; Provisional |
75-428 |
1.33e-05 |
|
xylulokinase; Provisional
Pssm-ID: 184987 [Multi-domain] Cd Length: 484 Bit Score: 47.65 E-value: 1.33e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 75 VKSIGIDTWGVDFGLIDKHGNLLGNPVCYRDARTEgipeEVFKLLDER--QHYADTGIQVMAINTLFQLYSMKQHQDAQL 152
Cdd:PRK15027 68 VKALGIAGQMHGATLLDAQQRVLRPAILWNDGRCA----QECALLEARvpQSRVITGNLMMPGFTAPKLLWVQRHEPEIF 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 153 EVARQLLFMPDLFSYFLTGVANNEYCIASTSELLDAQSRNWSVDTIRALGLPEHLFGEIILPGTIRGTLKEDIARETGLG 232
Cdd:PRK15027 144 RQIDKVLLPKDYLRLRMTGEFASDMSDAAGTMWLDVAKRDWSDVMLQACHLSRDQMPALYEGSEITGALLPEVAKAWGMA 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 233 TVDVIAvGSHDTASAVAAVPAVENPIAFLSSGTwSLLGVEVDEPILTEEarkaqftnEGGVDGkirFLQNITGLWILQRL 312
Cdd:PRK15027 224 TVPVVA-GGGDNAAGAVGVGMVDANQAMLSLGT-SGVYFAVSEGFLSKP--------ESAVHS---FCHALPQRWHLMSV 290
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 313 MSEWKACGE-------EQNYDIIIPQAAEAQIATiipvDDATFM-------NPENMENA------LIHycrHHAlqvpkn 372
Cdd:PRK15027 291 MLSAASCLDwaakltgLSNVPALIAAAQQADESA----EPVWFLpylsgerTPHNNPQAkgvffgLTH---QHG------ 357
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*.
gi 1697055883 373 KAETVRCVLQSLAFKYRQAVEQLNHCLPSPiRQLNIIGGGSQNQLLNQLTADELGI 428
Cdd:PRK15027 358 PNELARAVLEGVGYALADGMDVVHACGIKP-QSVTLIGGGARSEYWRQMLADISGQ 412
|
|
| ASKHA_NBD_FGGY_RBK-like |
cd07768 |
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family ... |
13-472 |
4.98e-04 |
|
nucleotide-binding domain (NBD) of ribulokinase-like carbohydrate kinases; The RBK family includes bacterial RBK, vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein), Saccharomyces cerevisiae D-ribulokinase YDR109C, and Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. RBK (EC 2.7.1.16; also known as L-ribulokinase) catalyzes the MgATP-dependent phosphorylation of L(or D)-ribulose to produce L(or D)-ribulose 5-phosphate and ADP, which is the second step in arabinose catabolism. It also phosphorylates a variety of other sugar substrates including ribitol and arabitol. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466788 [Multi-domain] Cd Length: 522 Bit Score: 42.61 E-value: 4.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 13 DFGGGSGRIIAGFLHHGkLELEEVYRFCNRQVKLGNHIYWDFP-----ALFEDMKTGLKLAAQKGYAVKSIGIDTwGVDF 87
Cdd:cd07768 6 DVGTSSARAGVYDLYAG-LEMAQEPVPYYQDSSKKSWKFWQKSteiikALQKCVQKLNIREGVDAYEVKGCGVDA-TCSL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 88 GLIDKHGNLL-----GNP----VCYRDART----EGIPEEVFKLLDERqhYADTGIQVMAINTLFQLysmKQHQDAQLEV 154
Cdd:cd07768 84 AIFDREGTPLmalipYPNednvIFWMDHSAvneaQWINMQCPQQLLDY--LGGKISPEMGVPKLKYF---LDEYSHLRDK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 155 ARQLLFMPDLFSYFLTGVANNEYCIASTSELLDAQSRNWSVDTIRALGLP-EHLFGEIILP-----GTIRGTLKEDIARE 228
Cdd:cd07768 159 HFHIFDLHDYIAYELTRLYEWNICGLLGKENLDGEESGWSSSFFKNIDPRlEHLTTTKNLPsnvpiGTTSGVALPEMAEK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 229 TGLGTVDVIAVGSHDTASAVAAVPAVENPIA-FLSSGTWS--LLGVEVDEPI-----LTEEARKAQFT-NEGGvdgkirf 299
Cdd:cd07768 239 MGLHPGTAVVVSCIDAHASWFAVASPHLETSlFMIAGTSSchMYGTTISDRIpgvwgPFDTIIDPDYSvYEAG------- 311
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 300 lQNITGL---WILQRLMSeWKACGEEQNYDIIIPQAAEAQIATIIPV---------------DDATFMNPeNMENALIHY 361
Cdd:cd07768 312 -QSATGKlieHLFESHPC-ARKFDEALKKGADIYQVLEQTIRQIEKNnglsihiltldmffgNRSEFADP-RLKGSFIGE 388
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1697055883 362 crhhALQV-PKNKAETVRCVLQSLAFKYRQAVEQLNHcLPSPIRQLNIIGGGSQNQLLNQLTADELGIPV-YAGPVEATA 439
Cdd:cd07768 389 ----SLDTsMLNLTYKYIAILEALAFGTRLIIDTFQN-EGIHIKELRASGGQAKNERLLQLIALVTNVAIiKPKENMMGI 463
|
490 500 510
....*....|....*....|....*....|....*....
gi 1697055883 440 MGNILTQAMAKG--EIADLRELREI----VTRSVTPQVY 472
Cdd:cd07768 464 LGAAVLAKVAAGkkQLADSITEADIsndrKSETFEPLAY 502
|
|
| ASKHA_NBD_FGGY_D-RBK |
cd07782 |
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily ... |
381-431 |
4.33e-03 |
|
nucleotide-binding domain (NBD) of D-ribulokinase FGGY and similar proteins; The subfamily includes vertebrate D-ribulokinase FGGY (also known as FGGY carbohydrate kinase domain-containing protein) and similar proteins, such as Saccharomyces cerevisiae D-ribulokinase YDR109C, Yersinia Pseudotuberculosis uncharacterized carbohydrate kinase that has been named glyerol/xylulose kinase. D-ribulokinase (EC 2.7.1.47) catalyzes ATP-dependent phosphorylation of D-ribulose at C-5 to form D-ribulose 5-phosphate. It is postulated to function in a metabolite repair mechanism by preventing toxic accumulation of free D-ribulose formed by non-specific phosphatase activities. Alternatively, D-ribulokinase may play a role in regulating D-ribulose 5-phosphate recycling in the pentose phosphate pathway.
Pssm-ID: 466800 [Multi-domain] Cd Length: 540 Bit Score: 39.44 E-value: 4.33e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1697055883 381 LQSLAFKYRQAVEQLN---HclpsPIRQLNIIGGGSQNQLLNQLTADELGIPVY 431
Cdd:cd07782 423 LQALAYGTRHIIEAMNaagH----KIDTIFMCGGLSKNPLFVQLHADVTGCPVV 472
|
|
| |
